Q8FY98 (HIS8_BRUSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histidinol-phosphate aminotransferase
EC=2.6.1.9

Alternative name(s):
Imidazole acetol-phosphate transaminase

Gene names

Name:	hisC
Ordered Locus Names:	BR1987, BS1330_I1981

Organism

Brucella suis biovar 1 (strain 1330) [Complete proteome] [HAMAP]

Taxonomic identifier

204722 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella

Protein attributes

Sequence length	365 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	L-histidinol phosphate + 2-oxoglutarate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate. HAMAP MF_01023
Cofactor	Pyridoxal phosphate By similarity. HAMAP MF_01023
Pathway	Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9. HAMAP MF_01023
Subunit structure	Homodimer By similarity. HAMAP MF_01023
Sequence similarities	Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Histidine biosynthesis
Ligand	Pyridoxal phosphate
Molecular function	Aminotransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	histidine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	1-aminocyclopropane-1-carboxylate synthase activity Inferred from electronic annotation. Source: InterPro L-phenylalanine:2-oxoglutarate aminotransferase activity Inferred from electronic annotation. Source: EC histidinol-phosphate transaminase activity Inferred from electronic annotation. Source: EC pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 365	365	Histidinol-phosphate aminotransferase HAMAP MF_01023		PRO_0000153328
Amino acid modifications
	Modified residue	223	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8FY98 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: 6EDBFD0D7B8E2694	FASTA	365	39,967
	10 20 30 40 50 60 MQKPTRPQPK AGVLDIAAYV PGKEHVEGVA KVYKLSSNET PLGPSPHARE AYRHAGEKLE 70 80 90 100 110 120 LYPDGQALAL RQAIAETQGL NISNILCGNG SDELLGLLCQ TYLAPGDETI ITEHGFAVYK 130 140 150 160 170 180 IQTLAAGATP VTVKEKNERI DVDAILAGVT ARTKIVFIAN PANPTGTYLP FEEVRRLHAG 190 200 210 220 230 240 LPQHVLLVLD AAYAEYVRRN DYEAGLELVS SNENVVMTRT FSKIHGLPGL RIGWIYAPLH 250 260 270 280 290 300 IIDAMNRIRG PFNMNSAAIA AGAAAIRDRA HVEKSVAYNE KWLAWLTEEF TRLGLRVTPS 310 320 330 340 350 360 VTNFLLIHFP DDAAHSADKA DEWLSRRGYI LRRVGGYGFP NALRMTVGPE EANRGVVAAL TEFLK

References

[1]

"The Brucella suis genome reveals fundamental similarities between animal and plant pathogens and symbionts." Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F., Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Nelson W.C., Ayodeji B., Kraul M. , Shetty J., Malek J.A., Van Aken S.E., Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L., Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M. Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002) [PubMed: 12271122] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1330.

[2]

"Revised genome sequence of Brucella suis 1330." Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R. J. Bacteriol. 193:6410-6410(2011) [PubMed: 22038969] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1330.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE014291 Genomic DNA. Translation: AAN30877.1. CP002997 Genomic DNA. Translation: AEM19294.1.
RefSeq	NP_698962.1. NC_004310.3.
3D structure databases
ProteinModelPortal	Q8FY98.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1167688.
GenomeReviews	Gene locus BR1987 in contig AE014291_GR.
KEGG	bms:BR1987.
PATRIC	17792403. VBIBruSui107850_2024.
TIGR	BR1987.
Phylogenomic databases
HOGENOM	HBG646350.
OMA	GFLVYRI.
PhylomeDB	Q8FY98.
ProtClustDB	PRK02731.
Enzyme and pathway databases
BioCyc	BSUI204722:BR_1987-MONOMER.
Family and domain databases
HAMAP	MF_01023. HisC_aminotrans_2. [Tree]
InterPro	IPR001176. ACC_synthase. IPR004839. Aminotransferase_I/II. IPR005861. HisP_aminotrans. IPR015424. PyrdxlP-dep_Trfase_major_dom. IPR015421. PyrdxlP-dep_Trfase_major_sub1. IPR015422. PyrdxlP-dep_Trfase_major_sub2. [Graphical view]
Gene3D	G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit. G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 1 hit.
KO	K00817.
Pfam	PF00155. Aminotran_1_2. 1 hit. [Graphical view]
PRINTS	PR00753. ACCSYNTHASE.
SUPFAM	SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
TIGRFAMs	TIGR01141. HisC. 1 hit.
PROSITE	PS00599. AA_TRANSFER_CLASS_2. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HIS8_BRUSU

Accession

Primary (citable) accession number: Q8FY98
Secondary accession number(s): G0K8K7

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 7, 2003
Last sequence update:	March 1, 2003
Last modified:	January 25, 2012
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program